-
1
-
-
0036525715
-
Oxidative biotransformations using oxygenases
-
This overview describes considerable progress in oxidative biotransformations using oxygenases (hydroxylation, Baeyer-Villiger oxidation, epoxidation, peroxidation and dihydroxylation)
-
Li Z., van Beilen J.B., Duetz W.A., Schmid A., de Raadt A., Griengl H., Witholt B. Oxidative biotransformations using oxygenases. Curr Opin Chem Biol. 6:2002;136-144. This overview describes considerable progress in oxidative biotransformations using oxygenases (hydroxylation, Baeyer-Villiger oxidation, epoxidation, peroxidation and dihydroxylation).
-
(2002)
Curr Opin Chem Biol
, vol.6
, pp. 136-144
-
-
Li, Z.1
Van Beilen, J.B.2
Duetz, W.A.3
Schmid, A.4
De Raadt, A.5
Griengl, H.6
Witholt, B.7
-
2
-
-
0035818010
-
Synthesis of a broad array of highly functionalized, enantiomerically pure cyclohexanecarboxylic acid derivatives by microbial dihydroxylation of benzoic acid and subsequent oxidative and rearrangement reactions
-
Myers A.G., Siegel D.R., Buzard D.J., Charest M.G. Synthesis of a broad array of highly functionalized, enantiomerically pure cyclohexanecarboxylic acid derivatives by microbial dihydroxylation of benzoic acid and subsequent oxidative and rearrangement reactions. Org Lett. 3:2001;2923-2926.
-
(2001)
Org Lett
, vol.3
, pp. 2923-2926
-
-
Myers, A.G.1
Siegel, D.R.2
Buzard, D.J.3
Charest, M.G.4
-
3
-
-
0032039678
-
Cytochrome P450 monooxygenases
-
Wong L.L. Cytochrome P450 monooxygenases. Curr Opin Chem Biol. 2:1998;263-268.
-
(1998)
Curr Opin Chem Biol
, vol.2
, pp. 263-268
-
-
Wong, L.L.1
-
4
-
-
0034572736
-
Cytochromes P450: A success story
-
This review provides general information about gene organization, structural features, localization and function. It also gives information on the enzyme mechanism of cytochromes P450 and defines the major unsolved issues in this field
-
Werck-Reichhart D., Feyereisen R. Cytochromes P450: a success story. Genome Biol. 1:2000;3003. This review provides general information about gene organization, structural features, localization and function. It also gives information on the enzyme mechanism of cytochromes P450 and defines the major unsolved issues in this field.
-
(2000)
Genome Biol
, vol.1
, pp. 3003
-
-
Werck-Reichhart, D.1
Feyereisen, R.2
-
5
-
-
0036525713
-
Protein engineering of oxygenases for biocatalysis
-
A new review presenting progress in the protein engineering of oxygenases. The authors give some interesting examples of changing the substrate specificity and stereoselectivity of monooxygenases, dioxygenases and chloroperoxidases
-
Cirino P.C., Arnold F.H. Protein engineering of oxygenases for biocatalysis. Curr Opin Chem Biol. 6:2002;130-135. A new review presenting progress in the protein engineering of oxygenases. The authors give some interesting examples of changing the substrate specificity and stereoselectivity of monooxygenases, dioxygenases and chloroperoxidases.
-
(2002)
Curr Opin Chem Biol
, vol.6
, pp. 130-135
-
-
Cirino, P.C.1
Arnold, F.H.2
-
6
-
-
0022919721
-
Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
-
Poulos T.L., Finzel B.C., Howard A.J. Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry. 25:1986;5314-5322.
-
(1986)
Biochemistry
, vol.25
, pp. 5314-5322
-
-
Poulos, T.L.1
Finzel, B.C.2
Howard, A.J.3
-
7
-
-
0031013972
-
The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
-
Li H., Poulos T.L. The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat Struct Biol. 4:1997;140-146.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 140-146
-
-
Li, H.1
Poulos, T.L.2
-
8
-
-
0028282737
-
Crystallization and preliminary X-ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum
-
Nakahara K., Shoun H., Adachi S., Iizuka T., Shiro Y. Crystallization and preliminary X-ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum. J Mol Biol. 239:1994;158-159.
-
(1994)
J Mol Biol
, vol.239
, pp. 158-159
-
-
Nakahara, K.1
Shoun, H.2
Adachi, S.3
Iizuka, T.4
Shiro, Y.5
-
10
-
-
0029586252
-
Structure of cytochrome P450eryF involved in erythromycin biosynthesis
-
Cupp-Vickery J.R., Poulos T.L. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat Struct Biol. 2:1995;144-153.
-
(1995)
Nat Struct Biol
, vol.2
, pp. 144-153
-
-
Cupp-Vickery, J.R.1
Poulos, T.L.2
-
11
-
-
0033823623
-
Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus
-
Park S.Y., Yamane K., Adachi S., Shiro Y., Weiss K.E., Sligar S.G. Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus. Acta Crystallogr D Biol Crystallogr. 56:2000;1173-1175.
-
(2000)
Acta Crystallogr D Biol Crystallogr
, vol.56
, pp. 1173-1175
-
-
Park, S.Y.1
Yamane, K.2
Adachi, S.3
Shiro, Y.4
Weiss, K.E.5
Sligar, S.G.6
-
12
-
-
0034738973
-
Microsomal cytochrome P450 2C5: Comparison to microbial P450s and unique features
-
Williams P.A., Cosme J., Sridhar V., Johnson E.F., McRee D.E. Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features. J Inorg Biochem. 81:2000;183-190.
-
(2000)
J Inorg Biochem
, vol.81
, pp. 183-190
-
-
Williams, P.A.1
Cosme, J.2
Sridhar, V.3
Johnson, E.F.4
McRee, D.E.5
-
13
-
-
0035853108
-
Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors
-
Podust L.M., Poulos T.L., Waterman M.R. Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. Proc Natl Acad Sci USA. 98:2001;3068-3073.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 3068-3073
-
-
Podust, L.M.1
Poulos, T.L.2
Waterman, M.R.3
-
14
-
-
0023645035
-
High-resolution crystal structure of cytochrome P450cam
-
Poulos T.L., Finzel B.C., Howard A.J. High-resolution crystal structure of cytochrome P450cam. J Mol Biol. 195:1987;687-700.
-
(1987)
J Mol Biol
, vol.195
, pp. 687-700
-
-
Poulos, T.L.1
Finzel, B.C.2
Howard, A.J.3
-
15
-
-
85031365167
-
Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus
-
Oct 24; epub ahead of print
-
Yano JK, Blasco F, Li H, Schmid RD, Henne A, Poulos TL: Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus. J Biol Chem 2002 Oct 24; epub ahead of print.
-
(2002)
J Biol Chem
-
-
Yano, J.K.1
Blasco, F.2
Li, H.3
Schmid, R.D.4
Henne, A.5
Poulos, T.L.6
-
16
-
-
85031357456
-
2.3 Å crystal structure of Streptomyces coelicolor CYP154C1: Insight into diversity of macrolide monooxygenases
-
22-30 June, Moscow, Russia; Abstract CO1_3.2
-
Podust LM, Waterman MR: 2.3 Å crystal structure of Streptomyces coelicolor CYP154C1: insight into diversity of macrolide monooxygenases. International Conference on Genomics, Proteomics and Bioinformatics for Medicine, 22-30 June 2002, Moscow, Russia; Abstract CO1_3.2.
-
(2002)
International Conference on Genomics, Proteomics and Bioinformatics for Medicine
-
-
Podust, L.M.1
Waterman, M.R.2
-
17
-
-
0035893679
-
Modelling of three-dimensional structures of cytochromes P450 11B1 and 11B2
-
Belkina N.V., Lisurek M., Ivanov A.S., Bernhardt R. Modelling of three-dimensional structures of cytochromes P450 11B1 and 11B2. J Inorg Biochem. 87:2001;197-207.
-
(2001)
J Inorg Biochem
, vol.87
, pp. 197-207
-
-
Belkina, N.V.1
Lisurek, M.2
Ivanov, A.S.3
Bernhardt, R.4
-
18
-
-
0035856564
-
Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3
-
Ost T.W., Miles C.S., Munro A.W., Murdoch J., Reid G.A., Chapman S.K. Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3. Biochemistry. 40:2001;13421-13429.
-
(2001)
Biochemistry
, vol.40
, pp. 13421-13429
-
-
Ost, T.W.1
Miles, C.S.2
Munro, A.W.3
Murdoch, J.4
Reid, G.A.5
Chapman, S.K.6
-
19
-
-
0035856538
-
Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3
-
Ost T.W., Munro A.W., Mowat C.G., Taylor P.R., Pesseguiero A., Fulco A.J., Cho A.K., Cheesman M.A., Walkinshaw M.D., Chapman S.K. Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3. Biochemistry. 40:2001;13430-13438.
-
(2001)
Biochemistry
, vol.40
, pp. 13430-13438
-
-
Ost, T.W.1
Munro, A.W.2
Mowat, C.G.3
Taylor, P.R.4
Pesseguiero, A.5
Fulco, A.J.6
Cho, A.K.7
Cheesman, M.A.8
Walkinshaw, M.D.9
Chapman, S.K.10
-
20
-
-
0035940433
-
Probing the open state of cytochrome P450cam with ruthenium-linker substrates
-
Dunn A.R., Dmochowski I.J., Bilwes A.M., Gray H.B., Crane B.R. Probing the open state of cytochrome P450cam with ruthenium-linker substrates. Proc Natl Acad Sci USA. 98:2001;12420-12425.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 12420-12425
-
-
Dunn, A.R.1
Dmochowski, I.J.2
Bilwes, A.M.3
Gray, H.B.4
Crane, B.R.5
-
21
-
-
0034681370
-
Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes
-
Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.Y., Nakamura H., Adachi S., Shoun H., Shiro Y. Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes. J Biol Chem. 275:2000;4816-4826.
-
(2000)
J Biol Chem
, vol.275
, pp. 4816-4826
-
-
Shimizu, H.1
Obayashi, E.2
Gomi, Y.3
Arakawa, H.4
Park, S.Y.5
Nakamura, H.6
Adachi, S.7
Shoun, H.8
Shiro, Y.9
-
22
-
-
0032728219
-
Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3)
-
Li H., Poulos T.L. Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3). Biochim Biophys Acta. 1441:1999;141-149.
-
(1999)
Biochim Biophys Acta
, vol.1441
, pp. 141-149
-
-
Li, H.1
Poulos, T.L.2
-
23
-
-
0035856545
-
Pivotal role of water in the mechanism of P450BM-3
-
This paper describes the crystal structure of P45BM-3 with bound N-palmitoylglycine at a resolution of 1.65 Å. Such a high resolution allows us to understand the early steps of catalysis in P450s and revealed the role of a water molecule in substrate binding
-
Haines D.C., Tomchick D.R., Machius M., Peterson J.A. Pivotal role of water in the mechanism of P450BM-3. Biochemistry. 40:2001;13456-13465. This paper describes the crystal structure of P45BM-3 with bound N-palmitoylglycine at a resolution of 1.65 Å. Such a high resolution allows us to understand the early steps of catalysis in P450s and revealed the role of a water molecule in substrate binding.
-
(2001)
Biochemistry
, vol.40
, pp. 13456-13465
-
-
Haines, D.C.1
Tomchick, D.R.2
Machius, M.3
Peterson, J.A.4
-
24
-
-
0036005635
-
Crystallization and preliminary X-ray diffraction analysis of fatty-acid hydroxylase cytochrome P450BSβ from Bacillus subtilis
-
Lee D.S., Yamada A., Matsunaga I., Ichihara K., Adachi S., Park S.Y., Shiro Y. Crystallization and preliminary X-ray diffraction analysis of fatty-acid hydroxylase cytochrome P450BSβ from Bacillus subtilis. Acta Crystallogr D Biol Crystallogr. 58:2002;687-689.
-
(2002)
Acta Crystallogr D Biol Crystallogr
, vol.58
, pp. 687-689
-
-
Lee, D.S.1
Yamada, A.2
Matsunaga, I.3
Ichihara, K.4
Adachi, S.5
Park, S.Y.6
Shiro, Y.7
-
25
-
-
0035476449
-
Site-directed mutagenesis of the putative distal helix of peroxygenase cytochrome P450
-
Matsunaga I., Ueda A., Sumimoto T., Ichihara K., Ayata M., Ogura H. Site-directed mutagenesis of the putative distal helix of peroxygenase cytochrome P450. Arch Biochem Biophys. 394:2001;45-53.
-
(2001)
Arch Biochem Biophys
, vol.394
, pp. 45-53
-
-
Matsunaga, I.1
Ueda, A.2
Sumimoto, T.3
Ichihara, K.4
Ayata, M.5
Ogura, H.6
-
26
-
-
0037169558
-
Complex formation of cytochrome P450cam with putidaredoxin. Evidence for protein-specific interactions involving the proximal thiolate ligand
-
Unno M., Christian J.F., Sjodin T., Benson D.E., Macdonald I.D., Sligar S.G., Champion P.M. Complex formation of cytochrome P450cam with putidaredoxin. Evidence for protein-specific interactions involving the proximal thiolate ligand. J Biol Chem. 277:2002;2547-2553.
-
(2002)
J Biol Chem
, vol.277
, pp. 2547-2553
-
-
Unno, M.1
Christian, J.F.2
Sjodin, T.3
Benson, D.E.4
Macdonald, I.D.5
Sligar, S.G.6
Champion, P.M.7
-
27
-
-
0036188282
-
A scanning tunneling microscopy (STM) investigation of complex formation between cytochrome P450(cam) and putidaredoxin
-
Djuricic D., Hill H.A., Lo K.K., Wong L.L. A scanning tunneling microscopy (STM) investigation of complex formation between cytochrome P450(cam) and putidaredoxin. J Inorg Biochem. 88:2002;362-367.
-
(2002)
J Inorg Biochem
, vol.88
, pp. 362-367
-
-
Djuricic, D.1
Hill, H.A.2
Lo, K.K.3
Wong, L.L.4
-
28
-
-
0033579488
-
The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site
-
Sevrioukova I.F., Hazzard J.T., Tollin G., Poulos T.L. The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site. J Biol Chem. 274:1999;36097-36106.
-
(1999)
J Biol Chem
, vol.274
, pp. 36097-36106
-
-
Sevrioukova, I.F.1
Hazzard, J.T.2
Tollin, G.3
Poulos, T.L.4
-
29
-
-
0037157130
-
Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119
-
The hydroxylation of lauric acid by the P450 enzyme from S. solfotaricus was supported by electron transfer from putidaredoxin reductase and putidaredoxin. This fatty acid activity was increased by site-directed mutagenesis, which increased putidaredoxin binding
-
Koo L.S., Immoos C.E., Cohen M.S., Farmer P.J., Ortiz De Montellano P.R. Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119. J Am Chem Soc. 124:2002;5684-5691. The hydroxylation of lauric acid by the P450 enzyme from S. solfotaricus was supported by electron transfer from putidaredoxin reductase and putidaredoxin. This fatty acid activity was increased by site-directed mutagenesis, which increased putidaredoxin binding.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 5684-5691
-
-
Koo, L.S.1
Immoos, C.E.2
Cohen, M.S.3
Farmer, P.J.4
Ortiz De Montellano, P.R.5
-
30
-
-
0036134828
-
Molecular Lego: Design of molecular assemblies of P450 enzymes for nanobiotechnology
-
Demonstration of the successful application of the molecular Lego approach to P450 enzymes with three objectives: to build an artificial multidomain redox chain, to construct soluble human P450 enzyme, and to create a library of new P459 BM-3 mutants
-
Gilardi G., Meharenna Y.T., Tsotsou G.E., Sadeghi S.J., Fairhead M., Giannini S. Molecular Lego: design of molecular assemblies of P450 enzymes for nanobiotechnology. Biosens Bioelectron. 17:2002;133-145. Demonstration of the successful application of the molecular Lego approach to P450 enzymes with three objectives: to build an artificial multidomain redox chain, to construct soluble human P450 enzyme, and to create a library of new P459 BM-3 mutants.
-
(2002)
Biosens Bioelectron
, vol.17
, pp. 133-145
-
-
Gilardi, G.1
Meharenna, Y.T.2
Tsotsou, G.E.3
Sadeghi, S.J.4
Fairhead, M.5
Giannini, S.6
-
32
-
-
0028979829
-
Electrocatalytically driven ω-hydroxylation of fatty acids using cytochrome P450 4A1
-
Faulkner K.M., Shet M.S., Fisher C.W., Estabrook R.W. Electrocatalytically driven ω-hydroxylation of fatty acids using cytochrome P450 4A1. Proc Natl Acad Sci USA. 92:1995;7705-7709.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 7705-7709
-
-
Faulkner, K.M.1
Shet, M.S.2
Fisher, C.W.3
Estabrook, R.W.4
-
33
-
-
0034727799
-
P450 in biotechnology: Zinc driven ω-hydroxylation of π-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst
-
This paper describes the application of zinc dust for the regeneration of the mediator cobalt sepulchrate, which can replace the NADPH cofactor
-
Schwaneberg U., Appel D., Schmitt J., Schmid R.D. P450 in biotechnology: zinc driven ω-hydroxylation of π-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst. J Biotechnol. 84:2000;249-257. This paper describes the application of zinc dust for the regeneration of the mediator cobalt sepulchrate, which can replace the NADPH cofactor.
-
(2000)
J Biotechnol
, vol.84
, pp. 249-257
-
-
Schwaneberg, U.1
Appel, D.2
Schmitt, J.3
Schmid, R.D.4
-
34
-
-
0036165342
-
Photochemical properties of a riboflavins/cytochrome P450 2B4 complex
-
Very interesting example in which the photochemical properties of riboflavins are used to obtain a non-covalent complex with one artificial flavocytochrome P4502B4. After the introduction of the flavin residue the cytochrome P450 enzyme can be used as a photodiode or photoreceptor
-
Shumyantseva V.V., Bulko T.V., Schmid R.D., Archakov A.I. Photochemical properties of a riboflavins/cytochrome P450 2B4 complex. Biosens Bioelectron. 17:2002;233-238. Very interesting example in which the photochemical properties of riboflavins are used to obtain a non-covalent complex with one artificial flavocytochrome P4502B4. After the introduction of the flavin residue the cytochrome P450 enzyme can be used as a photodiode or photoreceptor.
-
(2002)
Biosens Bioelectron
, vol.17
, pp. 233-238
-
-
Shumyantseva, V.V.1
Bulko, T.V.2
Schmid, R.D.3
Archakov, A.I.4
-
35
-
-
0344348884
-
A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A
-
Schwaneberg U., Schmidt-Dannert C., Schmitt J., Schmid R.D. A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Anal Biochem. 269:1999;359-366.
-
(1999)
Anal Biochem
, vol.269
, pp. 359-366
-
-
Schwaneberg, U.1
Schmidt-Dannert, C.2
Schmitt, J.3
Schmid, R.D.4
-
36
-
-
0035037955
-
Cost-effective whole-cell assay for laboratory evolution of hydroxylases in Escherichia coli
-
Schwaneberg U., Otey C., Cirino P.C., Farinas E., Arnold F.H. Cost-effective whole-cell assay for laboratory evolution of hydroxylases in Escherichia coli. J Biomol Screen. 6:2001;111-117.
-
(2001)
J Biomol Screen
, vol.6
, pp. 111-117
-
-
Schwaneberg, U.1
Otey, C.2
Cirino, P.C.3
Farinas, E.4
Arnold, F.H.5
-
37
-
-
0036136872
-
High-throughput assay for cytochrome P450 BM3 for screening libraries of substrates and combinatorial mutants
-
Tsotsou G.E., Cass A.E., Gilardi G. High-throughput assay for cytochrome P450 BM3 for screening libraries of substrates and combinatorial mutants. Biosens Bioelectron. 17:2002;119-131.
-
(2002)
Biosens Bioelectron
, vol.17
, pp. 119-131
-
-
Tsotsou, G.E.1
Cass, A.E.2
Gilardi, G.3
-
38
-
-
0035900342
-
Residue size at position 87 of cytochrome P450 BM-3 determines its stereoselectivity in propylbenzene and 3-chlorostyrene oxidation
-
Li Q.S., Ogawa J., Schmid R.D., Shimizu S. Residue size at position 87 of cytochrome P450 BM-3 determines its stereoselectivity in propylbenzene and 3-chlorostyrene oxidation. FEBS Lett. 508:2001;249-252.
-
(2001)
FEBS Lett
, vol.508
, pp. 249-252
-
-
Li, Q.S.1
Ogawa, J.2
Schmid, R.D.3
Shimizu, S.4
-
39
-
-
0035501591
-
Modification of the fatty acid specificity of cytochrome P450BM-3 from Bacillus megaterium by directed evolution: A validated assay
-
Lentz O., Li Q.-S., Schwaneberg U., Lutz-Wahl S., Fischer P., Schmid R.D. Modification of the fatty acid specificity of cytochrome P450BM-3 from Bacillus megaterium by directed evolution: a validated assay. J Mol Catal B Enzym. 15:2001;123-133.
-
(2001)
J Mol Catal B Enzym
, vol.15
, pp. 123-133
-
-
Lentz, O.1
Li, Q.-S.2
Schwaneberg, U.3
Lutz-Wahl, S.4
Fischer, P.5
Schmid, R.D.6
-
40
-
-
0035876716
-
A P450 BM-3 mutant hydroxylates alkanes, cycloalkanes, arenes and heteroarenes
-
Short report about the extraordinary substrate specificity of a CYP102 mutant
-
Appel D., Lutz-Wahl S., Fischer P., Schwaneberg U., Schmid R.D. A P450 BM-3 mutant hydroxylates alkanes, cycloalkanes, arenes and heteroarenes. J Biotechnol. 88:2001;167-171. Short report about the extraordinary substrate specificity of a CYP102 mutant.
-
(2001)
J Biotechnol
, vol.88
, pp. 167-171
-
-
Appel, D.1
Lutz-Wahl, S.2
Fischer, P.3
Schwaneberg, U.4
Schmid, R.D.5
-
41
-
-
0035661021
-
Engineering the CYP101 system for in vivo oxidation of unnatural substrates
-
This paper describes a functional in vivo catalytic system based on CYP101 and its cofactor proteins and indicates the great facility of this system for directed evolution of CYP101. The authors report the construction of new mutants with enhanced activity for unusual substrates
-
Bell S.G., Harford-Cross C.F., Wong L.L. Engineering the CYP101 system for in vivo oxidation of unnatural substrates. Protein Eng. 14:2001;797-802. This paper describes a functional in vivo catalytic system based on CYP101 and its cofactor proteins and indicates the great facility of this system for directed evolution of CYP101. The authors report the construction of new mutants with enhanced activity for unusual substrates.
-
(2001)
Protein Eng
, vol.14
, pp. 797-802
-
-
Bell, S.G.1
Harford-Cross, C.F.2
Wong, L.L.3
-
42
-
-
0035859869
-
Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: Enzymatic, crystallographic, and theoretical studies
-
French K.J., Strickler M.D., Rock D.A., Bennett G.A., Wahlstrom J.L., Goldstein B.M., Jones J.P. Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies. Biochemistry. 40:2001;9532-9538.
-
(2001)
Biochemistry
, vol.40
, pp. 9532-9538
-
-
French, K.J.1
Strickler, M.D.2
Rock, D.A.3
Bennett, G.A.4
Wahlstrom, J.L.5
Goldstein, B.M.6
Jones, J.P.7
-
43
-
-
0037085236
-
Active site mutations of cytochrome p450cam alter the binding, coupling, and oxidation of the foreign substrates (R)- and (S)-2-ethylhexanol
-
French K.J., Rock D.A., Manchester J.I., Goldstein B.M., Jones J.P. Active site mutations of cytochrome p450cam alter the binding, coupling, and oxidation of the foreign substrates (R)- and (S)-2-ethylhexanol. Arch Biochem Biophys. 398:2002;188-197.
-
(2002)
Arch Biochem Biophys
, vol.398
, pp. 188-197
-
-
French, K.J.1
Rock, D.A.2
Manchester, J.I.3
Goldstein, B.M.4
Jones, J.P.5
-
44
-
-
0035830723
-
Rational evolution of a medium-chain-specific cytochrome P-450 BM-3 variant
-
Li Q.S., Schwaneberg U., Fischer M., Schmitt J., Pleiss J., Lutz-Wahl S., Schmid R.D. Rational evolution of a medium-chain-specific cytochrome P-450 BM-3 variant. Biochim Biophys Acta. 1545:2001;114-121.
-
(2001)
Biochim Biophys Acta
, vol.1545
, pp. 114-121
-
-
Li, Q.S.1
Schwaneberg, U.2
Fischer, M.3
Schmitt, J.4
Pleiss, J.5
Lutz-Wahl, S.6
Schmid, R.D.7
-
45
-
-
0001122596
-
Directed evolution of a cytochrome P450 monooxygenase for alkane oxidation
-
Farinas E.T., Schwaneberg U., Glieder A., Arnold F.H. Directed evolution of a cytochrome P450 monooxygenase for alkane oxidation. Adv Synth Catal. 343:2001;601-606.
-
(2001)
Adv Synth Catal
, vol.343
, pp. 601-606
-
-
Farinas, E.T.1
Schwaneberg, U.2
Glieder, A.3
Arnold, F.H.4
-
46
-
-
4243244912
-
Prospecting for proteins
-
Wilson E.K. Prospecting for proteins. Chem Eng News. 17:2001;49-51.
-
(2001)
Chem Eng News
, vol.17
, pp. 49-51
-
-
Wilson, E.K.1
-
47
-
-
0034595354
-
Directed evolution of the fatty-acid hydroxylase P450 BM-3 into an indole-hydroxylating catalyst
-
Li Q.S., Schwaneberg U., Fischer P., Schmid R.D. Directed evolution of the fatty-acid hydroxylase P450 BM-3 into an indole-hydroxylating catalyst. Chemistry. 6:2000;1531-1536.
-
(2000)
Chemistry
, vol.6
, pp. 1531-1536
-
-
Li, Q.S.1
Schwaneberg, U.2
Fischer, P.3
Schmid, R.D.4
-
48
-
-
0029758268
-
Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 1A1, 1A2, and epoxide hydrolase
-
Shou M., Gonzalez F.J., Gelboin H.V. Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 1A1, 1A2, and epoxide hydrolase. Biochemistry. 35:1996;15807-15813.
-
(1996)
Biochemistry
, vol.35
, pp. 15807-15813
-
-
Shou, M.1
Gonzalez, F.J.2
Gelboin, H.V.3
-
49
-
-
0034069318
-
Protein engineering of cytochrome p450(cam) (CYP101) for the oxidation of polycyclic aromatic hydrocarbons
-
Harford-Cross C.F., Carmichael A.B., Allan F.K., England P.A., Rouch D.A., Wong L.L. Protein engineering of cytochrome p450(cam) (CYP101) for the oxidation of polycyclic aromatic hydrocarbons. Protein Eng. 13:2000;121-128.
-
(2000)
Protein Eng
, vol.13
, pp. 121-128
-
-
Harford-Cross, C.F.1
Carmichael, A.B.2
Allan, F.K.3
England, P.A.4
Rouch, D.A.5
Wong, L.L.6
-
50
-
-
0034819837
-
Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons
-
Using the protein engineering of P450 BM-3, new biocatalysts have been obtained with improved activity for PAH oxidation. Structural changes during substrate binding have been analyzed and the effect of different mutations on NADPH turnover and coupling efficiency has been described
-
Carmichael A.B., Wong L.L. Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons. Eur J Biochem. 268:2001;3117-3125. Using the protein engineering of P450 BM-3, new biocatalysts have been obtained with improved activity for PAH oxidation. Structural changes during substrate binding have been analyzed and the effect of different mutations on NADPH turnover and coupling efficiency has been described.
-
(2001)
Eur J Biochem
, vol.268
, pp. 3117-3125
-
-
Carmichael, A.B.1
Wong, L.L.2
-
51
-
-
0035653258
-
Engineering cytochrome P450 BM-3 for oxidation of polycyclic aromatic hydrocarbons
-
Li Q.S., Ogawa J., Schmid R.D., Shimizu S. Engineering cytochrome P450 BM-3 for oxidation of polycyclic aromatic hydrocarbons. Appl Environ Microbiol. 67:2001;5735-5739.
-
(2001)
Appl Environ Microbiol
, vol.67
, pp. 5735-5739
-
-
Li, Q.S.1
Ogawa, J.2
Schmid, R.D.3
Shimizu, S.4
-
52
-
-
0033578095
-
Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
-
Joo H., Lin Z., Arnold F.H. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature. 399:1999;670-673.
-
(1999)
Nature
, vol.399
, pp. 670-673
-
-
Joo, H.1
Lin, Z.2
Arnold, F.H.3
-
53
-
-
0036842594
-
Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase
-
Glieder A., Farinas E.T., Arnold F.H. Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase. Nat Biotechnol. 20:2002;1135-1139.
-
(2002)
Nat Biotechnol
, vol.20
, pp. 1135-1139
-
-
Glieder, A.1
Farinas, E.T.2
Arnold, F.H.3
|